What is she best known for?
The fields of study she is best known for:
Her main research concerns Biochemistry, Arabidopsis, Ubiquitin ligase, Ubiquitin and Gene.
Her study on Mutant, Amino acid, Protein degradation and Luciferase is often connected to Low protein as part of broader study in Biochemistry.
Her work carried out in the field of Ubiquitin ligase brings together such families of science as Arabidopsis thaliana, Kinase and Ankyrin repeat.
Her Ubiquitin research integrates issues from Proteasome and Cell biology.
Judy Callis combines subjects such as CUL1, NEDD8 and Multiprotein complex with her study of Cell biology.
Her Gene study is related to the wider topic of Genetics.
Her most cited work include:
- Functional Analysis of the RING-Type Ubiquitin Ligase Family of Arabidopsis (442 citations)
- Interactions of the COP9 Signalosome with the E3 Ubiquitin Ligase SCF TIR1 in Mediating Auxin Response (407 citations)
- Ubiquitin, hormones and biotic stress in plants. (402 citations)
What are the main themes of her work throughout her whole career to date?
Judy Callis mainly focuses on Biochemistry, Ubiquitin, Ubiquitin ligase, Arabidopsis and Cell biology.
When carried out as part of a general Biochemistry research project, her work on Proteolysis, Protein degradation, Luciferase and Amino acid is frequently linked to work in Fusion protein, therefore connecting diverse disciplines of study.
Judy Callis has included themes like Plasma protein binding and Proteasome in her Ubiquitin study.
Her Ubiquitin ligase study integrates concerns from other disciplines, such as Transcription factor and DNA-binding protein.
Her Arabidopsis research includes elements of Arabidopsis thaliana, Gene expression and Molecular biology.
The Cell biology study combines topics in areas such as Receptor, Protein subunit, Auxin and Jasmonate.
She most often published in these fields:
- Biochemistry (59.21%)
- Ubiquitin (50.00%)
- Ubiquitin ligase (46.05%)
What were the highlights of her more recent work (between 2010-2021)?
- Ubiquitin ligase (46.05%)
- Biochemistry (59.21%)
- Arabidopsis (42.11%)
In recent papers she was focusing on the following fields of study:
Judy Callis spends much of her time researching Ubiquitin ligase, Biochemistry, Arabidopsis, Ubiquitin and Arabidopsis thaliana.
Her research is interdisciplinary, bridging the disciplines of Cell biology and Ubiquitin ligase.
Her Cell biology research incorporates themes from Damaged DNA binding, Protein subunit and Auxin.
Her Arabidopsis research is multidisciplinary, incorporating perspectives in Abscisic acid and Nucleoside.
Her Ubiquitin research incorporates elements of Amino acid, Proteolysis and Proteasome.
The various areas that Judy Callis examines in her Arabidopsis thaliana study include Chloroplast, Kinase and Ribose, Ribokinase.
Between 2010 and 2021, her most popular works were:
- The ubiquitination machinery of the ubiquitin system. (136 citations)
- IRT1 DEGRADATION FACTOR1, a RING E3 Ubiquitin Ligase, Regulates the Degradation of IRON-REGULATED TRANSPORTER1 in Arabidopsis (95 citations)
- ABA and the ubiquitin E3 ligase KEEP ON GOING affect proteolysis of the Arabidopsis thaliana transcription factors ABF1 and ABF3. (83 citations)
In her most recent research, the most cited papers focused on:
The scientist’s investigation covers issues in Ubiquitin ligase, Biochemistry, Arabidopsis, Ubiquitin and Arabidopsis thaliana.
Her Ubiquitin ligase research focuses on Jasmonate and how it connects with Endoplasmic-reticulum-associated protein degradation, Cell biology, Endoplasmic reticulum, Receptor and Protein biosynthesis.
Her studies deal with areas such as Transcription factor and Abscisic acid as well as Arabidopsis.
Her Ubiquitin research focuses on Proteolysis and how it relates to Proteases, Proteasome and Vacuole.
Her work deals with themes such as Transport protein, Xenopus, Plasma protein binding and DNA-binding protein, which intersect with Arabidopsis thaliana.
Her Mutant research is multidisciplinary, relying on both Plastid, Gene expression and Transcription.
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